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PXD006574

PXD006574 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAn Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding
DescriptionApolipoprotein (apo)A-I mediates many of the anti-atherogenic functions attributed to high density lipoprotein (HDL). Unfortunately, efforts toward a high-resolution structure of full-length apoA-I have not been fruitful, though there have been successes with deletion mutants. Recently, a C-terminal truncation (apoA-IΔ185-243) was crystallized as a dimer. The structure showed two helical bundles connected by a long, curved pair of swapped helical domains. To compare this structure to that existing under solution conditions, we applied small angle X-ray scattering and isotope-assisted chemical cross-linking to apoA-IΔ185-243 in its dimeric and monomeric forms. For the dimer, we found evidence for the shared domains and aspects of the N-terminal bundles, but not the molecular curvature seen in the crystal. We also found that the N-terminal bundles equilibrate between open and closed states. Interestingly, this movement is one of the transitions proposed during lipid binding. The monomer was consistent with a model in which the long shared helix doubles back onto the helical bundle. Combined with the crystal structure, these data offer an important starting point to understand the molecular details of HDL biogenesis.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:38:16.626.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD006574
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterDiogo Borges Lima
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListOxidation
InstrumentTripleTOF 5600
Dataset History
RevisionDatetimeStatusChangeLog Entry
02017-05-23 05:55:08ID requested
12017-05-30 07:38:08announced
22024-10-22 04:38:18announced2024-10-22: Updated project metadata.
Publication List
10.1074/jbc.M115.706093;
10.6019/PXD006574;
Melchior JT, Walker RG, Morris J, Jones MK, Segrest JP, Lima DB, Carvalho PC, Gozzo FC, Castleberry M, Thompson TB, Davidson WS, An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding. J Biol Chem, 291(10):5439-51(2016) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: apolipoprotein, mass spectrometry (MS), structural biology, oligomerization, small-angle X-ray scattering (SAXS),structural model
Contact List
Paulo C Carvalho
contact affiliationComputational Mass Spectrometry Group - Brazil
contact emailpaulo@pcarvalho.com
lab head
Diogo Borges Lima
contact affiliationLeibniz-Forschungsinstitut für Molekulare Pharmakologie
contact emaildiogobor@gmail.com
dataset submitter
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Dataset FTP location
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